Protein Modifications and Regulation

These flashcards cover key vocabulary related to protein modifications, their functions, and regulatory mechanisms as discussed in the lecture.

Protein Modification

Alterations made to proteins that can change their activity, stability, or solubility.

Ubiquitin

A small protein that can be covalently attached to other proteins to tag them for degradation by the proteasome.

Proteasome

A large multi-protein complex that degrades unneeded, damaged, or misfolded proteins.

ATP Hydrolysis

A chemical reaction that breaks down ATP, often providing energy for various cellular processes, including protein regulation.

Ligand Binding

The interaction between a ligand and a protein, where the strength of binding can influence the activity and functionality of the protein.

GTP vs GDP

GTP (guanosine triphosphate) binds to proteins to activate them, while GDP (guanosine diphosphate) binds to deactivate them.

Acidic and Basic Conditions

Environments that can affect protein interactions based on the charges present in the solvent and amino acids.

Covalent Modification

The chemical alteration of a protein through the formation of covalent bonds, affecting its function and stability.

Regulated Degradation

The controlled process of breaking down proteins, allowing precise time-dependent regulation during cellular processes.

Mutations and Protein Function

Alterations in the protein sequence that can lead to different functional outcomes depending on the specific context.